TETW_BUTFI
ID TETW_BUTFI Reviewed; 639 AA.
AC O52836;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Tetracycline resistance protein TetW;
DE Short=Tet(W);
GN Name=tetW; Synonyms=tet(W);
OS Butyrivibrio fibrisolvens.
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=831;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1.230;
RX PubMed=9292992; DOI=10.1128/aem.63.9.3405-3411.1997;
RA Scott K.P., Barbosa T.M., Forbes K.J., Flint H.J.;
RT "High-frequency transfer of a naturally occurring chromosomal tetracycline
RT resistance element in the ruminal anaerobe Butyrivibrio fibrisolvens.";
RL Appl. Environ. Microbiol. 63:3405-3411(1997).
CC -!- FUNCTION: Abolishes the inhibitory effect of tetracyclin on protein
CC synthesis by a non-covalent modification of the ribosomes.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. TetM/TetO
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR EMBL; AJ222769; CAA10975.1; -; Genomic_DNA.
DR RefSeq; WP_002586627.1; NG_048281.1.
DR AlphaFoldDB; O52836; -.
DR SMR; O52836; -.
DR GeneID; 64114426; -.
DR KEGG; ag:CAA10975; -.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR CDD; cd03711; Tet_C; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR035650; Tet_C.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF03764; EFG_IV; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00889; EFG_IV; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance; GTP-binding; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..639
FT /note="Tetracycline resistance protein TetW"
FT /id="PRO_0000091516"
FT DOMAIN 1..243
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 74..78
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 128..131
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 639 AA; 71295 MW; 9043F095B9CF38B5 CRC64;
MKIINIGILA HVDAGKTTLT ESLLYASGAI SEPGSVEKGT TRTDTMFLER QRGITIQAAV
TSFQWHRCKV NIVDTPGHMD FLAEVYRSLA VLDGAILVIS AKDGVQAQTR ILFHALRKMN
IPTVIFINKI DQAGVDLQSV VQSVRDKLSA DIIIKQTVSL SPEIVLEENT DIEAWDAVIE
NNDELLEKYI AGEPISREKL AREEQQRVQD ASLFPVYHGS AKNGLGIQPL MDAVTGLFQP
IGEQGGAALC GSVFKVEYTD CGQRRVYLRL YSGTLRLRDT VALAGREKLK ITEMRIPSKG
EIVRTDTAYQ GEIVILPSDS VRLNDVLGDQ TRLPRKRWRE DPLPMLRTTI APKTAAQRER
LLDALTQLAD TDPLLRCEVD SITHEIILSF LGRVQLEVVS ALLSEKYKLE TVVKEPSVIY
MERPLKAASH TIHIEVPPNP FWASIGLSVT PLSLGSGVQY ESRVSLGYLN QSFQNAVRDG
IRYGLEQGLF GWNVTDCKIC FEYGLYYSPV STPADFRSLA PIVLEQALKE SGTQLLEPYL
SFILYAPQEY LSRAYHDAPK YCATIETAQV KKDEVVFTGE IPARCIQAYR TDLAFYTNGR
SVCLTELKGY QAAVGQPVIQ PRRPNSRLDK VRHMFQKVM